Analysis of equilibrium binding of an orthosteric tracer and two allosteric modulators

• DOI: 10.1371/journal.pone.0214255
• Publication Date: 2019-03-27T20:43:24Z
• Authors: Jan Jakubík; Alena Randáková; Esam E. El-Fakahany; Vladimír Doležal
• Keywords: Allosteric modulator; Allosteric enzyme

Allosteric ligands bind to receptors at sites that are distinct from those endogenous agonists and orthosteric pharmacological agents interact with. Both an allosteric ligand simultaneously the receptor form a ternary complex, where each influences binding affinity of other receptor, either positively or negatively. modulators intensively studied group because their potentially greater selectivity over ligands, with possibility fine tuning effects neurotransmitters hormones. The unlabelled is commonly estimated by measuring its on radio-labelled tracer. This scenario complicated many folds when one studies kinetics interactions two agents, added simultaneously, In this paper, we provide, for first time, theoretical basis analysis such complex interactions. We have expanded our include having same different receptor. An value provide tool distinguish between situations. Finally, also modelled molecules modulator